scholarly journals The identification of a peptide in human parotid saliva particularly active in enhancing the glycolytic activity of the salivary micro-organisms

1975 ◽  
Vol 149 (2) ◽  
pp. 489-492 ◽  
Author(s):  
I B Holbrook ◽  
P C Molan
Keyword(s):  
Molecular Weight ◽  
Peptide Analysis ◽  
Parotid Saliva ◽  
Basic Peptide ◽  
Glycolytic Activity ◽  
Micro Organisms ◽  
Human Parotid Saliva

A factor in saliva responsible for markedly activating the glycolytic activity of micro-organisms was isolated from parotid secretions and identified as a small basic peptide. Analysis of the peptide showed a high proportion of histidine, lysine and arginine. Its minimum molecular weight was calculated to be between 2500 and 3000.

Characterization of Low-molecular-weight Peptides in Human Parotid Saliva

1995 ◽  
Vol 74 (1) ◽  
pp. 345-350 ◽  
Author(s):  
H.E.R. Perinpanayagam ◽  
B.C. VanWuyckhuyse ◽  
Z.S. Ji ◽  
L.A. Tabak
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Parotid Saliva ◽  
Human Parotid Saliva

Purification and Some Properties of Fucosyltransferase in Human Parotid Saliva

1987 ◽  
Vol 66 (1) ◽  
pp. 72-77 ◽  
Author(s):  
H. Tamagawa ◽  
E. Inoshita ◽  
T. Takeshita ◽  
M. Takagaki ◽  
S. Shizukuishi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Affinity Chromatography ◽  
Enzyme Activities ◽  
Chromatographic Analysis ◽  
Metal Ion ◽  
Divalent Metal ◽  
Parotid Saliva ◽  
Divalent Metal Ion ◽  
Human Parotid Saliva

Fucosyltransferase was purified from human parotid saliva by affinity chromatography on GDP-hexanolamine Sepharose, followed by chromatofocusing on PBE 94 exchanger gel. The purified enzyme had the N-acetylglucosaminide α1→4, the N-acetylglucosaminide α1→3, and the glucoside α1→3 fucosyltransferase activities. The molecular weight of the purified enzyme was estimated to be approximately 20,000. These enzyme activities showed identical pH and divalent metal ion dependencies and identical rates of inactivation upon being heated. The paper chromatographic analysis of the fucosylated products by the purified enzyme and the susceptibility of these products to linkage-specific fucosidase digestion indicated that the transferase formed the Fuc α1→4GlcNAc, Fuc α1→3GlcNAc, and Fuc α1→3Glc linkages.

Isolation and Characterization of β-N-Acetylglucosaminidase from Human Parotid Saliva

1973 ◽  
Vol 52 (4) ◽  
pp. 782-790 ◽  
Author(s):  
Tatsuo Watanabe ◽  
Ryo Nakamura ◽  
Yoshifumi Iwamoto ◽  
Akira Tsunemitsu
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Parotid Saliva ◽  
Disk Electrophoresis ◽  
Isolation And Characterization ◽  
Human Parotid Saliva ◽  
Cellulose Column

Beta-N-acetylglucosaminidase in human parotid saliva was separated into two subfractions by diethylaminoethanol cellulose column chromatography. One subfraction of the enzyme was isolated and purified. Disk electrophoresis showed that the purified enzyme was homogeneous. The molecular weight of this enzyme was estimated to be about 153,000 by gel filtration and dodecyl sulfate polyacrylamide gel electrophoresis. N-acetyl-β-galactosaminides also were hydrolyzed by this enzyme at the same site.

scholarly journals Chemical and physical characteristics of a phosphoprotein from human parotid saliva

1975 ◽  
Vol 145 (3) ◽  
pp. 557-567 ◽  
Author(s):  
A Bennick
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Magnetic Resonance ◽  
Protein A ◽  
Chemical Analyses ◽  
Terminal Sequence ◽  
Parotid Saliva ◽  
Ester Linkage ◽  
Human Parotid Saliva ◽  
Phenylalanine Residue

The isolation of a highly purified phosphoprotein, previously named protein A, from human parotid saliva is described. This protein has an unusually high amount of glycine, proline and dicarboxylic amino acids. Together these amino acids account for 80% of all residues. The protein contains 1.9mol of P/mol of protein, probably as phosphate in an ester linkage to serine, and about 0.5% carbohydrate, but no hexosamine. The N-terminal is blocked and the following C-terminal sequence is proposed: -Aal-Asp-Ser-Gln-Gly-Arg-Arg. The sioelectric point is 4.43. The molecular weight of the protein determined by ultracentrifugation is 9900 and from chemical analyses 11000. Circular-dichrosim and nuclea-magnetic-resonance spectra indicate the absence of polyproline and triple-helical-collagen-like structure for the protein. There is little restriction on the orientation of the single phenylalanine residue in the protein., but there is also an indication of conformational restraint in the protein.

Purification and Some Properties of a-L-Fucosidase Isolated from Streptococcus sanguis

1978 ◽  
Vol 57 (11-12) ◽  
pp. 1028-1035 ◽  
Author(s):  
S. Shizukuishi ◽  
T. Taniguchi ◽  
S. Shibata ◽  
R. Nakamura ◽  
A. Tsunemitsu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Parotid Saliva ◽  
Streptococcus Sanguis ◽  
Naturally Occurring ◽  
Human Parotid Saliva ◽  
Optimal Ph

α-L-Fucosidase acting on naturally occurring substrates was highly purified from the growth culture of Streptococcus sanguis ATCC 10557. The molecular weight of the enzyme was approximately 120,000 and the optimal pH was at 5.5. The purified enzyme showed specificity toward the linkage of α-(1→2) fucosides in oligosaccharides and glycoproteins. The enzyme released L-fucose from glycoprotein in human parotid saliva.

scholarly journals Fractionation of human parotid saliva proteins.

1978 ◽  
Vol 253 (20) ◽  
pp. 7556-7565 ◽  
Author(s):  
R.I. Henkin ◽  
R.E. Lippoldt ◽  
J. Bilstad ◽  
R.O. Wolf ◽  
C.K. Lum ◽  
...  
Keyword(s):  
Parotid Saliva ◽  
Human Parotid Saliva

Substrate Specificity of Fucosyltransferase Purified from Human Parotid Saliva

1987 ◽  
Vol 66 (3) ◽  
pp. 756-760 ◽  
Author(s):  
H. Tamagawa ◽  
K. Iwakura ◽  
A. Amano ◽  
S. Shizukuishi ◽  
A. Tsunemitsu
Keyword(s):  
Substrate Specificity ◽  
Parotid Saliva ◽  
Human Parotid Saliva

Studies on histidine-rich polypeptides from human parotid saliva

1976 ◽  
Vol 177 (2) ◽  
pp. 427-436 ◽  
Author(s):  
Bruce J. Baum ◽  
Janice L. Bird ◽  
David B. Millar ◽  
Robert W. Longton
Keyword(s):  
Parotid Saliva ◽  
Human Parotid Saliva
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